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Q1LU68 (METE_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

EC=2.1.1.14
Alternative name(s):
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Gene names
Name:metE
Ordered Locus Names:BCI_0017
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation By similarity. HAMAP MF_00172

Catalytic activity

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00172

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. HAMAP MF_00172

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7647645-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000017224

Sites

Metal binding6461Zinc By similarity
Metal binding6481Zinc By similarity
Metal binding7311Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LU68 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 2EDBEE7151AC2A4C

FASTA76487,406
        10         20         30         40         50         60 
MTILSHILGF PRIGLHRELK RAQESYWDGH ITQQQLLNTG RELRACHWQQ QKQAGLNMLP 

        70         80         90        100        110        120 
VGDFAWYDHV LTTSLMLDNV PVRHRNDDGS SNIDTLYRIG RGNAPTGQPV VASEMTKWFN 

       130        140        150        160        170        180 
TNYHYIVPEF TVGQQFRLGW TQLIEEVDEA LALGYNIKPI LLGPISYLWL GKAKEKHFDR 

       190        200        210        220        230        240 
LSLLSALLPV YQQILALLAQ RGIEWVQIDE PALVLELPTA WCNAYYDAYT DALQGYSKLL 

       250        260        270        280        290        300 
LTTYFDSIGH HLNIITNLSV HGLHVDLIAG NDDVEVLHRT LPSNWVLSAG VINGRNVWRA 

       310        320        330        340        350        360 
DLPSKFKQLR SLVGQRELWV GSSCSLLHSP IDLSIETRMD PEVKSWFAFT IQKCNELKLL 

       370        380        390        400        410        420 
CNALNRLDDT KYQAILADYS APLWARQTSE KVHNRQVKIR TEQITENHSQ RQQHYLDRIN 

       430        440        450        460        470        480 
VQRARFNLPI LPTTTIGSFP QTTAIRSLRL DLKSGRIDNE YYKNAICNHI KQAITEQDAL 

       490        500        510        520        530        540 
GLDVLVHGEA ERNDMVEYFG EHLNGFIFTQ NGWVQSYGSR CVKPPIIIGD ISRPKPITVE 

       550        560        570        580        590        600 
WAWYAQSLTQ KPVKGMLTGP VTILCWSFPR EDLDRKTIAR QIALALRDEV IDLENAGIGI 

       610        620        630        640        650        660 
IQIDEPALRE GLPLKYSAWK EYLTWAVEAF RLNAAVAKNN TQIHTHMCYS EFNDIMDSII 

       670        680        690        700        710        720 
AMDADVITIE TSRSNMKLLD TFKQYQYPND IGPGVYDIHS PNIPSEDDII QLLRKAAQVI 

       730        740        750        760 
PIKRLWVNPD CGLKTRTWLE TRKALSNMVN AAHKLRREEE YNRS 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14113.1.
RefSeqYP_588496.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LU68.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LU68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056528.
GenomeReviewsGene locus BCI_0017 in contig CP000238_GR.
KEGGbci:BCI_0017.
PATRIC21073521. VBIBauCic75062_0017.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHBG287495.
OMARNIWRAN.
PhylomeDBQ1LU68.
ProtClustDBPRK05222.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0017-MONOMER.

Family and domain databases

HAMAPMF_00172. Meth_synth.
[Tree]
InterProIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Methionine_synth.
[Graphical view]
KOK00549.
PfamPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsTIGR01371. Met_syn_B12ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMETE_BAUCH
AccessionPrimary (citable) accession number: Q1LU68
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families